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Cutting Edge: Induction of the Antigen-Processing Enzyme IFN--Inducible Lysosomal Thiol Reductase in Melanoma Cells Is STAT1-Dependent but CIITA-Independent¹

Department of Microbiology and Immunology and Walther Oncology Center, Indiana University School of Medicine, Indianapolis, IN 46202; and Walther Cancer Institute, Indianapolis, IN 46208

Presentation and CD4⁺ T cell responses to Ag in the context of MHC class II molecules require processing of native proteins into short peptide fragments. Within this pathway, IFN--inducible lysosomal thiol reductase (GILT) functions to catalyze thiol bond reduction, thus unfolding native protein Ag and facilitating further processing via cellular proteases. In contrast with professional APCs such as B cells, class II-positive human melanomas expressed relatively little to no GILT protein or mRNA. Tumor cell GILT expression was partially restored with IFN- treatment but unlike other genes required for class II Ag presentation, GILT was not regulated by CIITA. Rather, studies revealed STAT1 plays a direct role in IFN--inducible GILT expression. These results define a molecular mechanism for the uncoupled regulation of MHC class II genes and the processing enzyme GILT in human melanomas.

This article has been cited by other articles:

				R. L. Lackman and P. Cresswell Exposure of the Promonocytic Cell Line THP-1 to Escherichia coli Induces IFN-{gamma}-Inducible Lysosomal Thiol Reductase Expression by Inflammatory Cytokines J. Immunol., October 1, 2006; 177(7): 4833 - 4840. [Abstract] [Full Text] [PDF]